Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae

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• dc.contributor.author Vizarraga, David
• dc.contributor.author Mazzolini, Rocco
• dc.contributor.author Lluch-Senar, Maria 1982-
• dc.contributor.author Aparicio, David
• dc.date.accessioned 2020-11-16T06:55:45Z
• dc.date.available 2020-11-16T06:55:45Z
• dc.date.issued 2020
• dc.description.abstract Mycoplasma pneumoniae is a bacterial human pathogen that causes primary atypical pneumonia. M. pneumoniae motility and infectivity are mediated by the immunodominant proteins P1 and P40/P90, which form a transmembrane adhesion complex. Here we report the structure of P1, determined by X-ray crystallography and cryo-electron microscopy, and the X-ray structure of P40/P90. Contrary to what had been suggested, the binding site for sialic acid was found in P40/P90 and not in P1. Genetic and clinical variability concentrates on the N-terminal domain surfaces of P1 and P40/P90. Polyclonal antibodies generated against the mostly conserved C-terminal domain of P1 inhibited adhesion of M. pneumoniae, and serology assays with sera from infected patients were positive when tested against this C-terminal domain. P40/P90 also showed strong reactivity against human infected sera. The architectural elements determined for P1 and P40/P90 open new possibilities in vaccine development against M. pneumoniae infections.
• dc.description.sponsorship This work was supported by grants BFU2018-101265-B-100 (MINECO) to I.F., BIO2017-84166-R (MINECO) to J.P., and BES-2015-076104 (MINECO) to M.L.S., JSPS KAKENHI Grant Number JP25000013 to K.N., and a FEDER project from Instituto de Salud Carlos III (ISCIII, Acción Estratégica en Salud 2016).
• dc.format.mimetype application/pdf
• dc.identifier.citation Vizarraga D, Kawamoto A, Matsumoto U, Illanes R, Pérez-Luque R, Martín J et al. Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae. Nat Commun. 2020; 11(1):5188. DOI: 10.1038/s41467-020-18777-y
• dc.identifier.doi http://dx.doi.org/10.1038/s41467-020-18777-y
• dc.identifier.issn 2041-1723
• dc.identifier.uri http://hdl.handle.net/10230/45768
• dc.language.iso eng
• dc.publisher Nature Research
• dc.relation.ispartof Nat Commun. 2020; 11(1):5188
• dc.relation.projectID info:eu-repo/grantAgreement/ES/2PE/BFU2018-101265-B-100
• dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BIO2017-84166-R
• dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BES-2015-076104
• dc.rights © The Author(s) 2020. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
• dc.rights.accessRights info:eu-repo/semantics/openAccess
• dc.rights.uri http://creativecommons.org/licenses/by/4.0/
• dc.subject.keyword Electron microscopy
• dc.subject.keyword Immunology
• dc.subject.keyword Microbiology
• dc.subject.keyword Structural biology
• dc.subject.keyword X-ray crystallography
• dc.title Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae
• dc.type info:eu-repo/semantics/article
• dc.type.version info:eu-repo/semantics/publishedVersion